BMRB Entry 25487

Name: Purotoxin-2 NMR structure in DPC micelles
Published: 2016-04-12

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PDB ID: 2mzg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25487
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Purotoxin-2 NMR structure in DPC micelles

Deposition date:

2015-02-12

Original release date:

2016-04-12

Authors:

Nadezhdin, Kirill; Oparin, Peter; Vassilevski, Alexander; Grishin, Evgeny; Arseniev, Alexander

Citation:

Citation: Oparin, Peter; Nadezhdin, Kirill; Berkut, Antonina; Arseniev, Alexander; Grishin, Eugene; Vassilevski, Alexander. "Structure of purotoxin-2 from wolf spider: modular design and membrane-assisted mode of action in arachnid toxins." Biochem. J. 473, 3113-3126 (2016).
PubMed: 27412961

Assembly members:

Assembly members:
entity, polymer, 64 residues, 7278.426 Da.

Natural source:

Natural source: Common Name: Wolf spiders Taxonomy ID: 74999 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Alopecosa not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: AKACTPLLHDCSHDRHSCCR GDMFKYVCDCFYPEGEDKTE VCSCQQPKSHKIAEKIIDKA KTTL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	176
15N chemical shifts	62
1H chemical shifts	415

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 64 residues - 7278.426 Da.

1

ALA

LYS

ALA

CYS

THR

PRO

LEU

HIS

ASP

2

CYS

SER

HIS

ASP

ARG

HIS

SER

CYS

ARG

3

GLY

ASP

MET

PHE

LYS

TYR

VAL

CYS

ASP

CYS

4

PHE

TYR

PRO

GLU

GLY

GLU

ASP

LYS

THR

GLU

5

VAL

CYS

SER

CYS

GLN

PRO

LYS

SER

HIS

6

LYS

ILE

ALA

GLU

LYS

ILE

ASP

LYS

ALA

7

LYS

THR

LEU

Samples:

sample_1: entity, [U-100% 15N], 1 mM; DPC 100 mM; D2O 5%; H2O 95%

sample_conditions_1: pH: 3.3; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis, refinement

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks